› 6syu

X-ray diffraction
1.33Å resolution

The wild type glucuronoyl esterase OtCE15A from Opitutus terrae in complex with xylobiose

Released:
DOI: 10.2210/pdb6syu/pdb
PDB entry 6syu coloured by chain, front view.
PDB entry 6syu coloured by chain, side view.
PDB entry 6syu coloured by chain, top view.
Source organism: Opitutus terrae
Primary publication:
Structural and biochemical studies of the glucuronoyl esterase OtCE15A illuminate its interaction with lignocellulosic components.
Mazurkewich S, Poulsen JN, Lo Leggio L, Larsbrink J
J Biol Chem 294 19978-19987 (2019)
PMID: 31740581

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109476 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Putative acetyl xylan esterase Chain: A
Molecule details ›
Chain: A
Length: 421 amino acids
Theoretical weight: 46.15 KDa
Source organism: Opitutus terrae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B1ZMF4 (Residues: 33-432; Coverage: 96%)
Gene name: Oter_0116

Ligands and Environments

Carbohydrate polymer : NEW Components: XYP
Carbohydrate polymer
3 bound ligands:
Ligand MG 1 x MG
Ligand EDO 5 x EDO
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX IV BEAMLINE BioMAX
Spacegroup: P1
Unit cell:
a: 43.686Å b: 44.34Å c: 50.979Å
α: 77.236° β: 67.267° γ: 70.577°
R-values:
R R work R free
0.121 0.12 0.145
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Glucuronoyl esterases - enzymes to decouple lignin and carbohydrates and enable better utilization of renewable plant biomass.
Larsbrink et al. (2023)
1 more

1 mention without citation

Structural and biochemical studies of the glucuronoyl esterase OtCE15A illuminate its interaction with lignocellulosic components.
Mazurkewich et al. (2019)